Chemical Biology
Research areas
Targeting RNA with arginine rich photoswitchable peptides.
The research activities in Chemical Biology aim to promote a fundamental understanding of biological processes and to engineer new functions into biological systems. Enzyme catalysis is a particular focus area with the goals of probing reaction mechanisms, the role of protein dynamics and quantum mechanical effects, and tailoring substrate selectivity for synthetic chemistry purposes. Another facet of research is concerned with manipulating biomolecular interactions by triggering protein or nucleic acid conformational switching using small molecules or light.
Current projects include:
- photonic control of biomacromolecular structure to regulate cellular events
- enzymology of terpenoid biosynthesis and synthetic biology approaches for expansion of the pool of these secondary metabolites to include novel terpenoid-like compounds with applications as drugs or fragrances, in crop protection and as research tools
- the role of hydride tunnelling in enzyme catalysis using dihydrofolate reductase as a model system
- design and application of miniature enzymes
An inhibitor nestles in a binding pocket of the enzyme calpain.
- development of selective inhibitors of the enzyme calpain-1, a potential target for anti-inflammatory therapy in diseases such as rheumatoid arthritis elucidation of reaction mechanisms of light-dependent flavoproteins including the DNA photolyase family and the phototropin group
- chemical and enzymatic synthesis of flavins and their analogues as photoswitches and probes of reaction mechanism
- structural biology of the 26S proteasome which plays a key role in protein degradation
2-Fluorofarnesyl diphosphate - a synthetic substrate of δ-cadinene synthase and aristolochene synthase.
- structure and mechanism of pseudopalindrome cutting restriction endonucleases and CRISPR associated nucleases
- synthesis of amino acid building blocks for RNA binding peptides
- synthesis, screening and mass spectrometric analysis of nucleic acid-binding cyclic peptides.